Zinc in PDB 6sj2: Amidohydrolase, Ahs with 3-Haa

The structure of Amidohydrolase, Ahs with 3-Haa, PDB code: 6sj2 was solved by J.H.Naismith, H.Song, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	56.33 / 1.25
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	99.810, 118.890, 83.320, 90.00, 90.00, 90.00
R / Rfree (%)	16.5 / 17.8

The structure of Amidohydrolase, Ahs with 3-Haa also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Zinc atom in the Amidohydrolase, Ahs with 3-Haa (pdb code 6sj2). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Amidohydrolase, Ahs with 3-Haa, PDB code: 6sj2:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Amidohydrolase, Ahs with 3-Haa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Amidohydrolase, Ahs with 3-Haa within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn502 b:12.5 occ:1.00 O9 A:3HA501 2.0 15.0 1.0 NE2 A:HIS77 2.0 12.9 1.0 NE2 A:HIS75 2.0 12.2 1.0 NE2 A:HIS253 2.1 13.4 1.0 OD1 A:ASP345 2.4 16.4 1.0 C7 A:3HA501 2.8 15.7 1.0 CD2 A:HIS75 3.0 12.2 1.0 O8 A:3HA501 3.0 16.5 1.0 CE1 A:HIS77 3.0 13.7 1.0 CD2 A:HIS253 3.0 13.6 1.0 CD2 A:HIS77 3.1 12.7 1.0 CE1 A:HIS75 3.1 12.3 1.0 CE1 A:HIS253 3.2 14.4 1.0 CG A:ASP345 3.3 15.6 1.0 OD2 A:ASP345 3.7 15.5 1.0 O A:HOH783 4.0 27.5 1.0 NE2 A:HIS290 4.0 12.3 1.0 ND1 A:HIS77 4.1 14.0 1.0 C2 A:3HA501 4.1 15.4 1.0 CG A:HIS75 4.1 12.1 1.0 ND1 A:HIS75 4.2 12.7 1.0 CG A:HIS253 4.2 13.3 1.0 CG A:HIS77 4.2 13.0 1.0 ND1 A:HIS253 4.2 14.6 1.0 CB A:ASP345 4.4 15.4 1.0 CA A:ASP345 4.6 15.5 1.0 N10 A:3HA501 4.7 15.3 1.0 CE1 A:HIS290 4.7 12.1 1.0 CD2 A:HIS290 4.9 12.2 1.0 C3 A:3HA501 4.9 15.5 1.0

Zinc binding site 2 out of 2 in the Amidohydrolase, Ahs with 3-Haa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Amidohydrolase, Ahs with 3-Haa within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn503 b:11.6 occ:1.00 NE2 B:HIS77 2.0 11.6 1.0 O8 B:3HA501 2.0 13.7 1.0 NE2 B:HIS75 2.0 11.7 1.0 NE2 B:HIS253 2.1 11.7 1.0 OD1 B:ASP345 2.5 15.6 1.0 C7 B:3HA501 2.8 14.5 1.0 O9 B:3HA501 2.9 15.6 1.0 CD2 B:HIS75 3.0 11.6 1.0 CE1 B:HIS77 3.0 12.3 1.0 CD2 B:HIS253 3.0 11.7 1.0 CD2 B:HIS77 3.1 11.6 1.0 CE1 B:HIS75 3.1 12.2 1.0 CE1 B:HIS253 3.2 12.5 1.0 CG B:ASP345 3.3 14.1 1.0 OD2 B:ASP345 3.7 13.6 1.0 NE2 B:HIS290 4.0 12.0 1.0 O B:HOH734 4.0 26.1 1.0 ND1 B:HIS77 4.1 12.5 1.0 CG B:HIS75 4.1 11.2 1.0 C2 B:3HA501 4.1 14.3 1.0 ND1 B:HIS75 4.1 11.7 1.0 CG B:HIS253 4.2 11.3 1.0 CG B:HIS77 4.2 12.1 1.0 ND1 B:HIS253 4.2 12.2 1.0 CB B:ASP345 4.5 13.7 1.0 CA B:ASP345 4.6 13.8 1.0 O B:HOH840 4.7 25.7 1.0 N10 B:3HA501 4.7 14.1 1.0 CE1 B:HIS290 4.7 11.6 1.0 CD2 B:HIS290 4.8 11.8 1.0 C3 B:3HA501 4.9 14.2 1.0

H.Song, C.Rao, Z.Deng, Y.Yi, J.H.Naismith. The Biosynthetic Pathway of the Benzoxazole in Nataxazole Proceeds Via An Unstable Ester and Has Synthetic Utility. Angew.Chem.Int.Ed.Engl. 2020.
ISSN: ESSN 1521-3773
PubMed: 31903677
DOI: 10.1002/ANIE.201915685